4 results match your criteria Biocatalysis And Biotransformation[Journal]

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Improved soluble expression of the gene encoding amylolytic enzyme Amo45 by fusion with the mobile-loop-region of co-chaperonin GroES in

Biocatal Biotransformation 2013 Nov 25;31(6):335-342. Epub 2013 Nov 25.

Universität Stuttgart, Institut für Industrielle Genetik , Stuttgart , Germany.

The gene encoding the amylolytic enzyme Amo45, originating from a metagenomic project, was retrieved by a consensus primer-based approach for glycoside hydrolase (GH) family 57 enzymes. Family 57 contains mainly uncharacterized proteins similar to archaeal thermoactive amylopullulanases. For characterization of these family members soluble, active enzymes have to be produced in sufficient amounts. Read More

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http://www.tandfonline.com/doi/full/10.3109/10242422.2013.85
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http://dx.doi.org/10.3109/10242422.2013.858712DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017763PMC
November 2013
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Use of bacteria for rapid, pH-neutral, hydrolysis of the model hydrophobic carboxylic acid ester p-nitrophenyl picolinate.

Biocatal Biotransformation 2012 Aug;30(4):435-439

Department of Biology, California State University Northridge, Northridge, CA 91330, USA ; Department of Chemistry and Biochemistry, California State University Northridge, Northridge, CA 91330, USA.

Caulobacter crescentus, Escherichia coli and Bacillus subtilis cultures promote the hydrolysis of the model ester p-nitrophenyl picolinate (PNPP) at neutral pH with high efficiency. Hydrolysis is related to cell concentration, while the interaction of PNPP with both bacterial cells and their extracellular molecules is required for a maximum rate of PNPP hydrolysis in C. crescentus cultures. Read More

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http://dx.doi.org/10.3109/10242422.2012.702269DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3490430PMC
August 2012
2 Reads

Mannosylphosphodolichol synthase overexpression supports angiogenesis.

Biocatal Biotransformation 2010 Jan;28(1):90-98

Department of Biochemistry, School of Medicine, University of Puerto Rico, Medical Sciences Campus, San Juan, Puerto Rico, USA.

Mannosylphospho dolichol synthase (DPMS) plays a critical role in Glc(3)Man(9)GlcNAc(2)-PP-Dol (lipid-linked oligosaccharide, LLO) biosynthesis, an essential intermediate in asparagine-linked (N-linked) protein glycosylation. We have observed earlier that phosphorylation of DPMS increases the catalytic activity of the enzyme by increasing the V(max) as well as the enzyme turnover (k(cat)) without significantly changing the K(m) for GDP-mannose. As a result, LLO biosynthesis, turnover and protein N-glycosylation are increased. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2903885PMC
January 2010
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Isolation of autochthonous non-white rot fungi with potential for enzymatic upgrading of Venezuelan extra-heavy crude oil.

Biocatal Biotransformation 2007 Mar;25(2-4):341-349

Unidad de Biotecnología del Petróleo, Centro de Biotecnología, Fundación Instituto de Estudios Avanzados (IDEA), C/Hoyo de la Puerta-Baruta, Sartenejas, Caracas 1080, Venezuela.

The increasing world demand for fuels makes it necessary to exploit the largest reserve of extra-heavy crude oil (EHCO) of the Orinoco Oil Belt from Venezuela. We propose the use of extracellular oxidative enzymes, in particular, lignin-degrading enzyme systems (LDS) of fungi, for enzymatic improvement of EHCO. Autochthonous non-white rot fungal strains able to use EHCO, and several polycyclic aromatic hydrocarbons (PAHs) as sole carbon source and energy, were isolated from EHCO-polluted soils and identified as belonging to the genera Fusarium, Penicillium , Trichoderma , Aspergillus , Neosartorya, Pseudallescheria, Cladosporium, Pestalotiopsis , Phoma and Paecillomyces. Read More

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http://dx.doi.org/10.1080/10242420701379908DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2556186PMC
March 2007
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